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2.7.7.B4: adenylyltransferase UBA4

This is an abbreviated version!
For detailed information about adenylyltransferase UBA4, go to the full flat file.

Reaction

ATP
+
Urm1p-terminal-Gly
=
diphosphate
+
Urm1p-terminal-Gly-AMP

Synonyms

N-terminal domain of Uba4, nucleotide-binding domain of Uba4p, Uba4, Uba4p

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.B4 adenylyltransferase UBA4

Natural Substrates Products

Natural Substrates Products on EC 2.7.7.B4 - adenylyltransferase UBA4

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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + Urm1p-terminal-Gly
diphosphate + Urm1p-terminal-Gly-AMP
show the reaction diagram
Urm1p-terminal-Gly-AMP + Uba4-SSH
Urm1p-terminal-Gly-COSH + human MOCS2A-SH + AMP
show the reaction diagram
the N-terminal domain of Uba4 catalyzes the activation of Urm1 by formation of an acyl-adenylate bond. After adenylation, persulfurated Uba4 is able to form a thiocarboxylate group at the C-terminal glycine of Urm1. The formation of a thioester intermediate between Uba4 and Urm1 is not observed. The functional similarities between Uba4 and MOCS3 (protein essential for the biosynthesis of the molybdenum cofactor in human) further demonstrate the evolutionary link between ATP-dependent protein conjugation and ATP-dependent cofactor sulfuration
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